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10.1038/srep11840 http://scihub22266oqcxt.onion/10.1038/srep11840 C4485320!4485320 !26121966     free     free     free Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Warning: imagejpeg(C:\Inetpub\vhosts\kidney.de\httpdocs\phplern\26121966 .jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       Sci+Rep 2015 ; 5 (ä): 11840 Nephropedia Template TP {{tp|p=26121966 |t=2015. Acceleration of protein folding by four orders of magnitude through a single amino acid substitution |pdf=|usr=}}{{26121966 }} gab.com Text Acceleration of protein folding by four orders of magnitude through a single amino acid substitution JO: Sci Rep http://www.kidney.de/pget.php?&tw=1&pmid=26121966 #FOAvip Cis prolyl peptide bonds are conserved structural elements in numerous protein families, although their formation is energetically unfavorable, intrinsically slow and often rate-limiting for folding. Here we investigate the reasons underlying the conservation of the cis proline that is diagnostic for the fold of thioredoxin-like thiol-disulfide oxidoreductases. We show that replacement of the conserved cis proline in thioredoxin by alanine can accelerate spontaneous folding to the native, thermodynamically most stable state by more than four orders of magnitude. However, the resulting trans alanine bond leads to small structural rearrangements around the active site that impair the function of thioredoxin as catalyst of electron transfer reactions by more than 100-fold. Our data provide evidence for the absence of a strong evolutionary pressure to achieve intrinsically fast folding rates, which is most likely a consequence of proline isomerases and molecular chaperones that guarantee high in vivo folding rates and yields. Twit Text FOAVip Acceleration of protein folding by four orders of magnitude through a single amino acid substitution ????Sci Rep http://www.kidney.de/pget.php?&tw=1&pmid=26121966 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=26121966 #FOAvip English Wikipedia <ref>{{Cite pmid|26121966 }}</ref> Acceleration of protein folding by four orders of magnitude through a single amino acid substitution #MMPMID26121966 Roderer DJ ; Schärer MA ; Rubini M ; Glockshuber R Sci Rep 2015[Jun]; 5 (ä): 11840 PMID26121966 show ga Cis prolyl peptide bonds are conserved structural elements in numerous protein families, although their formation is energetically unfavorable, intrinsically slow and often rate-limiting for folding. Here we investigate the reasons underlying the conservation of the cis proline that is diagnostic for the fold of thioredoxin-like thiol-disulfide oxidoreductases. We show that replacement of the conserved cis proline in thioredoxin by alanine can accelerate spontaneous folding to the native, thermodynamically most stable state by more than four orders of magnitude. However, the resulting trans alanine bond leads to small structural rearrangements around the active site that impair the function of thioredoxin as catalyst of electron transfer reactions by more than 100-fold. Our data provide evidence for the absence of a strong evolutionary pressure to achieve intrinsically fast folding rates, which is most likely a consequence of proline isomerases and molecular chaperones that guarantee high in vivo folding rates and yields. |*Protein Folding [MESH] |Amino Acid Substitution [MESH] |Catalytic Domain [MESH] |Circular Dichroism [MESH] |Conserved Sequence [MESH] |Crystallography, X-Ray [MESH] |Escherichia coli [MESH] |Escherichia coli Proteins/*chemistry/genetics [MESH] |Isomerism [MESH] |Kinetics [MESH] |Models, Molecular [MESH] |Oxidation-Reduction [MESH] |Proline/chemistry [MESH] |Protein Structure, Secondary [MESH] |Thermodynamics [MESH]Acceleration of protein folding by four orders of magnitude through a (epmc).pdf DeepDyve Pubget Overpricing